Literature summary for 4.4.1.13 extracted from

Campanini, B.; Schiaretti, F.; Abbruzzetti, S.; Kessler, D.; Mozzarelli, A.
Sulfur mobilization in cyanobacteria: the catalytic mechanism of L-cystine C-S lyase (C-DES) from synechocystis (2006), J. Biol. Chem., 281, 38769-38780.

Search for more literature for 4.4.1.13

Cloned(Commentary)

Cloned (Comment)	Organism
-	Synechocystis sp. PCC 6714

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Synechocystis sp. PCC 6714

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1	-	cystine	estimated from steady-state measurements	Synechocystis sp. PCC 6714

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp. PCC 6714	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Synechocystis sp. PCC 6714

Storage Stability

Storage Stability	Organism
-80°C, 10 mM MOPS buffer, pH 6.5	Synechocystis sp. PCC 6714

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-cystine + H2O	-	Synechocystis sp. PCC 6714	L-thiocysteine + pyruvate + NH3	-	?
L-cystine + H2O	cystine is preferred over cysteine as substrate	Synechocystis sp. PCC 6714	L-thiocysteine + pyruvate + NH3	-	?

Subunits

Subunits	Comment	Organism
homodimer	-	Synechocystis sp. PCC 6714

Synonyms

Synonyms	Comment	Organism
L-cystine C-S lyase	-	Synechocystis sp. PCC 6714

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	bound by Lys-223 in the active site	Synechocystis sp. PCC 6714

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Release 2023.1 (January 2023)